P20594 (ANPRB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Atrial natriuretic peptide receptor 2
EC=4.6.1.2

Alternative name(s):
Atrial natriuretic peptide receptor type B
Short name=ANP-B
Short name=ANPR-B
Short name=NPR-B
Guanylate cyclase B
Short name=GC-B

Gene names

Name:	NPR2
Synonyms:	ANPRB

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1047 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Receptor for the C-type natriuretic peptide NPPC/CNP hormone. Has guanylate cyclase activity upon binding of its ligand. May play a role in the regulation of skeletal growth. Ref.9 Ref.11
Catalytic activity	GTP = 3',5'-cyclic GMP + diphosphate.
Subcellular location	Membrane; Single-pass type I membrane protein.
Post-translational modification	Phosphorylation of the protein kinase-like domain is required for full activation by CNP By similarity.
Involvement in disease	Acromesomelic dysplasia, Maroteaux type (AMDM) [MIM:602875]: An autosomal recessive acromesomelic chondrodysplasia. Acromesomelic chondrodysplasias are rare hereditary skeletal disorders characterized by short stature, very short limbsand hand/foot malformations. The severity of limb abnormalities increases from proximal to distal with profoundly affected hands and feet showing brachydactyly and/or rudimentary fingers (knob-like fingers). AMDM is characterized by axial skeletal involvement with wedging of vertebral bodies. In AMDM all skeletal elements are present but show abnormal rates of linear growth. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11
Sequence similarities	Belongs to the adenylyl cyclase class-4/guanylyl cyclase family. Contains 1 guanylate cyclase domain. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Osteogenesis cGMP biosynthesis
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Dwarfism
Domain	Signal Transmembrane Transmembrane helix
Ligand	GTP-binding Nucleotide-binding
Molecular function	Lyase Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	bone development Inferred from electronic annotation. Source: Compara cellular response to granulocyte macrophage colony-stimulating factor stimulus Inferred from expression pattern PubMed 14687666. Source: UniProtKB intracellular signal transduction Inferred from electronic annotation. Source: InterPro ossification Inferred from electronic annotation. Source: UniProtKB-KW receptor guanylyl cyclase signaling pathway Inferred from direct assay Ref.9. Source: UniProtKB regulation of blood pressure Traceable author statement Ref.2. Source: ProtInc
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Traceable author statement PubMed 1327579. Source: ProtInc
Molecular_function	ATP binding Inferred from electronic annotation. Source: Compara GTP binding Inferred from electronic annotation. Source: UniProtKB-KW guanylate cyclase activity Inferred from direct assay Ref.9. Source: UniProtKB hormone binding Inferred from physical interaction Ref.8Ref.9. Source: UniProtKB natriuretic peptide receptor activity Inferred from direct assay Ref.8Ref.9. Source: UniProtKB peptide hormone binding Inferred from electronic annotation. Source: Compara protein kinase activity Inferred from electronic annotation. Source: InterPro transmembrane signaling receptor activity Traceable author statement PubMed 1327579. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Long (identifier: P20594-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Short (identifier: P20594-2)

Also known as: NPR-BI;

The sequence of this isoform differs from the canonical sequence as follows:
     964-1047: PVCAGVVGLK...GERKGPPGLL → KADSHSSPSLHLSQTLPTCFFSKGQSVLGLLA

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Potential
	Chain	23 – 1047	1025	Atrial natriuretic peptide receptor 2		PRO_0000012364
Regions
	Topological domain	23 – 458	436	Extracellular Potential
	Transmembrane	459 – 478	20	Helical; Potential
	Topological domain	479 – 1047	569	Cytoplasmic Potential
	Domain	513 – 786	274	Protein kinase
	Domain	861 – 991	131	Guanylate cyclase
Amino acid modifications
	Modified residue	513	1	Phosphoserine Ref.12
	Modified residue	516	1	Phosphothreonine Ref.12
	Modified residue	518	1	Phosphoserine Ref.12
	Modified residue	523	1	Phosphoserine Ref.12
	Modified residue	526	1	Phosphoserine Ref.12
	Modified residue	529	1	Phosphothreonine Ref.12
	Glycosylation	24	1	N-linked (GlcNAc...) Potential
	Glycosylation	35	1	N-linked (GlcNAc...) Potential
	Glycosylation	161	1	N-linked (GlcNAc...) Potential
	Glycosylation	195	1	N-linked (GlcNAc...) Potential
	Glycosylation	244	1	N-linked (GlcNAc...) Potential
	Glycosylation	277	1	N-linked (GlcNAc...) Potential
	Glycosylation	349	1	N-linked (GlcNAc...) Potential
	Disulfide bond	75 ↔ 101		By similarity
	Disulfide bond	439		Interchain Probable
	Disulfide bond	448		Interchain Probable
Natural variations
	Alternative sequence	964 – 1047	84	PVCAG…PPGLL → KADSHSSPSLHLSQTLPTCF FSKGQSVLGLLA in isoform Short.		VSP_001810
	Natural variant	32	1	P → T in AMDM. Ref.11 Corresponds to variant rs28931581 [ dbSNP | Ensembl ].		VAR_022583
	Natural variant	115	1	W → G in AMDM; markedly deficient activity. Ref.11 Corresponds to variant rs28931582 [ dbSNP | Ensembl ].		VAR_022584
	Natural variant	176	1	D → E in AMDM. Ref.11 Corresponds to variant rs28929479 [ dbSNP | Ensembl ].		VAR_022585
	Natural variant	232	1	M → I. Ref.13 Corresponds to variant rs55747238 [ dbSNP | Ensembl ].		VAR_042219
	Natural variant	297	1	T → M in AMDM; markedly deficient activity. Ref.11		VAR_022586
	Natural variant	338	1	Y → C in AMDM. Ref.11		VAR_022587
	Natural variant	409	1	A → T in AMDM. Ref.11		VAR_022588
	Natural variant	413	1	G → E in AMDM; markedly deficient activity. Ref.11		VAR_022589
	Natural variant	708	1	Y → C in AMDM. Ref.11		VAR_022590
	Natural variant	771	1	Q → E. Corresponds to variant rs5816 [ dbSNP | Ensembl ].		VAR_011968
	Natural variant	776	1	R → W in AMDM. Ref.11		VAR_022591
	Natural variant	882	1	V → I. Ref.13 Corresponds to variant rs55700371 [ dbSNP | Ensembl ].		VAR_042220
	Natural variant	957	1	R → C in AMDM. Ref.11		VAR_022592
	Natural variant	959	1	G → A in AMDM. Ref.11		VAR_022593
Experimental info
	Sequence conflict	755	1	T → S in BAA81737. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified February 1, 1991. Version 1. Checksum: 817FB74D6B31F7EF	FASTA	1,047	117,022
	10 20 30 40 50 60 MALPSLLLLV AALAGGVRPP GARNLTLAVV LPEHNLSYAW AWPRVGPAVA LAVEALGRAL 70 80 90 100 110 120 PVDLRFVSSE LEGACSEYLA PLSAVDLKLY HDPDLLLGPG CVYPAASVAR FASHWRLPLL 130 140 150 160 170 180 TAGAVASGFS AKNDHYRTLV RTGPSAPKLG EFVVTLHGHF NWTARAALLY LDARTDDRPH 190 200 210 220 230 240 YFTIEGVFEA LQGSNLSVQH QVYAREPGGP EQATHFIRAN GRIVYICGPL EMLHEILLQA 250 260 270 280 290 300 QRENLTNGDY VFFYLDVFGE SLRAGPTRAT GRPWQDNRTR EQAQALREAF QTVLVITYRE 310 320 330 340 350 360 PPNPEYQEFQ NRLLIRARED FGVELGPSLM NLIAGCFYDG ILLYAEVLNE TIQEGGTRED 370 380 390 400 410 420 GLRIVEKMQG RRYHGVTGLV VMDKNNDRET DFVLWAMGDL DSGDFQPAAH YSGAEKQIWW 430 440 450 460 470 480 TGRPIPWVKG APPSDNPPCA FDLDDPSCDK TPLSTLAIVA LGTGITFIMF GVSSFLIFRK 490 500 510 520 530 540 LMLEKELASM LWRIRWEELQ FGNSERYHKG AGSRLTLSLR GSSYGSLMTA HGKYQIFANT 550 560 570 580 590 600 GHFKGNVVAI KHVNKKRIEL TRQVLFELKH MRDVQFNHLT RFIGACIDPP NICIVTEYCP 610 620 630 640 650 660 RGSLQDILEN DSINLDWMFR YSLINDLVKG MAFLHNSIIS SHGSLKSSNC VVDSRFVLKI 670 680 690 700 710 720 TDYGLASFRS TAEPDDSHAL YAKKLWTAPE LLSGNPLPTT GMQKADVYSF GIILQEIALR 730 740 750 760 770 780 SGPFYLEGLD LSPKEIVQKV RNGQRPYFRP SIDRTQLNEE LVLLMERCWA QDPAERPDFG 790 800 810 820 830 840 QIKGFIRRFN KEGGTSILDN LLLRMEQYAN NLEKLVEERT QAYLEEKRKA EALLYQILPH 850 860 870 880 890 900 SVAEQLKRGE TVQAEAFDSV TIYFSDIVGF TALSAESTPM QVVTLLNDLY TCFDAIIDNF 910 920 930 940 950 960 DVYKVETIGD AYMVVSGLPG RNGQRHAPEI ARMALALLDA VSSFRIRHRP HDQLRLRIGV 970 980 990 1000 1010 1020 HTGPVCAGVV GLKMPRYCLF GDTVNTASRM ESNGQALKIH VSSTTKDALD ELGCFQLELR 1030 1040 GDVEMKGKGK MRTYWLLGER KGPPGLL
	Isoform Short (NPR-BI) [UniParc]. Checksum: 745D41E451E0D7DF	FASTA	995	111,208
	10 20 30 40 50 60 MALPSLLLLV AALAGGVRPP GARNLTLAVV LPEHNLSYAW AWPRVGPAVA LAVEALGRAL 70 80 90 100 110 120 PVDLRFVSSE LEGACSEYLA PLSAVDLKLY HDPDLLLGPG CVYPAASVAR FASHWRLPLL 130 140 150 160 170 180 TAGAVASGFS AKNDHYRTLV RTGPSAPKLG EFVVTLHGHF NWTARAALLY LDARTDDRPH 190 200 210 220 230 240 YFTIEGVFEA LQGSNLSVQH QVYAREPGGP EQATHFIRAN GRIVYICGPL EMLHEILLQA 250 260 270 280 290 300 QRENLTNGDY VFFYLDVFGE SLRAGPTRAT GRPWQDNRTR EQAQALREAF QTVLVITYRE 310 320 330 340 350 360 PPNPEYQEFQ NRLLIRARED FGVELGPSLM NLIAGCFYDG ILLYAEVLNE TIQEGGTRED 370 380 390 400 410 420 GLRIVEKMQG RRYHGVTGLV VMDKNNDRET DFVLWAMGDL DSGDFQPAAH YSGAEKQIWW 430 440 450 460 470 480 TGRPIPWVKG APPSDNPPCA FDLDDPSCDK TPLSTLAIVA LGTGITFIMF GVSSFLIFRK 490 500 510 520 530 540 LMLEKELASM LWRIRWEELQ FGNSERYHKG AGSRLTLSLR GSSYGSLMTA HGKYQIFANT 550 560 570 580 590 600 GHFKGNVVAI KHVNKKRIEL TRQVLFELKH MRDVQFNHLT RFIGACIDPP NICIVTEYCP 610 620 630 640 650 660 RGSLQDILEN DSINLDWMFR YSLINDLVKG MAFLHNSIIS SHGSLKSSNC VVDSRFVLKI 670 680 690 700 710 720 TDYGLASFRS TAEPDDSHAL YAKKLWTAPE LLSGNPLPTT GMQKADVYSF GIILQEIALR 730 740 750 760 770 780 SGPFYLEGLD LSPKEIVQKV RNGQRPYFRP SIDRTQLNEE LVLLMERCWA QDPAERPDFG 790 800 810 820 830 840 QIKGFIRRFN KEGGTSILDN LLLRMEQYAN NLEKLVEERT QAYLEEKRKA EALLYQILPH 850 860 870 880 890 900 SVAEQLKRGE TVQAEAFDSV TIYFSDIVGF TALSAESTPM QVVTLLNDLY TCFDAIIDNF 910 920 930 940 950 960 DVYKVETIGD AYMVVSGLPG RNGQRHAPEI ARMALALLDA VSSFRIRHRP HDQLRLRIGV 970 980 990 HTGKADSHSS PSLHLSQTLP TCFFSKGQSV LGLLA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Differential activation by atrial and brain natriuretic peptides of two different receptor guanylate cyclases." Chang M.S., Lowe D.G., Lewis M., Hellmiss R., Chen E., Goeddel D.V. Nature 341:68-72(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE (ISOFORM LONG). Tissue: Brain.
[2]	"Structure of the type B human natriuretic peptide receptor gene and association of a novel microsatellite polymorphism with essential hypertension." Rehemudula D., Nakayama T., Soma M., Takahashi Y., Uwabo J., Sato M., Izumi Y., Kanmatsuse K., Ozawa Y. Circ. Res. 84:605-610(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Blood.
[3]	"cGMP-dependent and -independent inhibition of a K+ conductance by natriuretic peptides: molecular and functional studies in human proximal tubule cells." Hirsch J.R., Meyer M., Maegert H.-J., Forssmann W.-G., Mollerup S., Herter P., Weber G., Cermak R., Ankorina-Stark I., Schlatter E., Kruhoffer M. J. Am. Soc. Nephrol. 10:472-480(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT). Tissue: Kidney.
[4]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	NHLBI resequencing and genotyping service (RS&G) Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG). Tissue: Brain.
[8]	"Extracellular domain-IgG fusion proteins for three human natriuretic peptide receptors. Hormone pharmacology and application to solid phase screening of synthetic peptide antisera." Bennett B.D., Bennett G.L., Vitangcol R.V., Jewett J.R., Burnier J., Henzel W., Lowe D.G. J. Biol. Chem. 266:23060-23067(1991) [PubMed] [Europe PMC] [Abstract] Cited for: LIGAND-BINDING.
[9]	"Selective activation of the B natriuretic peptide receptor by C-type natriuretic peptide (CNP)." Koller K.J., Lowe D.G., Bennett G.L., Minamino N., Kangawa K., Matsuo H., Goeddel D.V. Science 252:120-123(1991) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"An unappreciated role for RNA surveillance." Hillman R.T., Green R.E., Brenner S.E. Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[11]	"Mutations in the transmembrane natriuretic peptide receptor NPR-B impair skeletal growth and cause acromesomelic dysplasia, type Maroteaux." Bartels C.F., Buekuelmez H., Padayatti P., Rhee D.K., van Ravenswaaij-Arts C., Pauli R.M., Mundlos S., Chitayat D., Shih L.-Y., Al-Gazali L.I., Kant S., Cole T., Morton J., Cormier-Daire V., Faivre L., Lees M., Kirk J., Mortier G.R. , Leroy J., Zabel B., Kim C.A., Crow Y., Braverman N.E., van den Akker F., Warman M.L. Am. J. Hum. Genet. 75:27-34(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, VARIANTS AMDM THR-32; GLY-115; GLU-176; MET-297; CYS-338; THR-409; GLU-413; CYS-708; TRP-776; CYS-957 AND ALA-959, CHARACTERIZATION OF VARIANTS AMDM GLY-115; MET-297 AND GLU-413.
[12]	"Mass spectrometric identification of phosphorylation sites in guanylyl cyclase A and B." Yoder A.R., Stone M.D., Griffin T.J., Potter L.R. Biochemistry 49:10137-10145(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-513; THR-516; SER-518; SER-523; SER-526 AND THR-529.
[13]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] ILE-232 AND ILE-882.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB005647 Genomic DNA. Translation: BAA81737.1. AJ005282 mRNA. Translation: CAA06466.1. AL133410 Genomic DNA. Translation: CAI10987.1. EU326311 Genomic DNA. Translation: ACA05920.1. EU326311 Genomic DNA. Translation: ACA05921.1. CH471071 Genomic DNA. Translation: EAW58338.1. CH471071 Genomic DNA. Translation: EAW58337.1. CH471071 Genomic DNA. Translation: EAW58339.1. CH471071 Genomic DNA. Translation: EAW58340.1. BC023017 mRNA. Translation: AAH23017.1.
IPI	IPI00024685. IPI00219001.
PIR	OYHUBR. S05514.
RefSeq	NP_003986.2. NM_003995.3.
UniGene	Hs.78518.
3D structure databases
ProteinModelPortal	P20594.
ModBase	Search...
Protein-protein interaction databases
IntAct	P20594. 1 interaction.
STRING	9606.ENSP00000341083.
PTM databases
PhosphoSite	P20594.
Polymorphism databases
DMDM	113916.
Proteomic databases
PaxDb	P20594.
PRIDE	P20594.
Protocols and materials databases
DNASU	4882.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000342694; ENSP00000341083; ENSG00000159899.
GeneID	4882.
KEGG	hsa:4882.
UCSC	uc003zyd.3. human.
Organism-specific databases
CTD	4882.
GeneCards	GC09P035792.
H-InvDB	HIX0034787.
HGNC	HGNC:7944. NPR2.
HPA	HPA011977.
MIM	108961. gene. 602875. phenotype.
neXtProt	NX_P20594.
Orphanet	40. Acromesomelic dysplasia, Maroteaux type.
PharmGKB	PA257.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOVERGEN	HBG051862.
InParanoid	P20594.
KO	K12324.
OMA	AAKSEHY.
OrthoDB	EOG4TF0JG.
Gene expression databases
ArrayExpress	P20594.
Bgee	P20594.
CleanEx	HS_NPR2.
Genevestigator	P20594.
GermOnline	ENSG00000159899. Homo sapiens.
Family and domain databases
Gene3D	3.30.70.1230. 1 hit.
InterPro	IPR001054. A/G_cyclase. IPR018297. A/G_cyclase_CS. IPR001828. ANF_lig-bd_rcpt. IPR011009. Kinase-like_dom. IPR001170. Ntpep_rcpt. IPR000719. Prot_kinase_cat_dom. IPR001245. Ser-Thr/Tyr_kinase_cat_dom. [Graphical view]
Pfam	PF01094. ANF_receptor. 1 hit. PF00211. Guanylate_cyc. 1 hit. PF07714. Pkinase_Tyr. 1 hit. [Graphical view]
PRINTS	PR00255. NATPEPTIDER.
SMART	SM00044. CYCc. 1 hit. [Graphical view]
SUPFAM	SSF55073. A/G_cyclase. 1 hit. SSF56112. Kinase_like. 1 hit.
PROSITE	PS00458. ANF_RECEPTORS. 1 hit. PS00452. GUANYLATE_CYCLASE_1. 1 hit. PS50125. GUANYLATE_CYCLASE_2. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P20594.
ChEMBL	CHEMBL1795.
ChiTaRS	NPR2. human.
DrugBank	DB01613. Erythrityl Tetranitrate. DB04899. Nesiritide.
GenomeRNAi	4882.
NextBio	18792.
SOURCE	Search...

Entry information

Entry name

ANPRB_HUMAN

Accession

Primary (citable) accession number: P20594
Secondary accession number(s): B0ZBF2 , B0ZBF3, D3DRP3, D3DRP4, O60871, Q4VAK7, Q5TCV2, Q8TA93, Q9UQ50

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	May 1, 2013
This is version 154 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.